ID A8MAZ8_CALMQ Unreviewed; 614 AA.
AC A8MAZ8;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=aldehyde ferredoxin oxidoreductase {ECO:0000256|ARBA:ARBA00012818};
DE EC=1.2.7.5 {ECO:0000256|ARBA:ARBA00012818};
GN OrderedLocusNames=Cmaq_1809 {ECO:0000313|EMBL:ABW02627.1};
OS Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS IC-167).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Caldivirga.
OX NCBI_TaxID=397948 {ECO:0000313|EMBL:ABW02627.1, ECO:0000313|Proteomes:UP000001137};
RN [1] {ECO:0000313|EMBL:ABW02627.1, ECO:0000313|Proteomes:UP000001137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167
RC {ECO:0000313|Proteomes:UP000001137};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Caldivirga maquilingensis IC-167.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = a
CC carboxylate + 3 H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:16421, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001714};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the AOR/FOR family.
CC {ECO:0000256|ARBA:ARBA00011032}.
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DR EMBL; CP000852; ABW02627.1; -; Genomic_DNA.
DR RefSeq; WP_012186846.1; NC_009954.1.
DR AlphaFoldDB; A8MAZ8; -.
DR STRING; 397948.Cmaq_1809; -.
DR GeneID; 5709088; -.
DR KEGG; cma:Cmaq_1809; -.
DR eggNOG; arCOG00706; Archaea.
DR HOGENOM; CLU_020364_1_0_2; -.
DR Proteomes; UP000001137; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0033726; F:aldehyde ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.569.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 2; 1.
DR Gene3D; 1.10.599.10; Aldehyde Ferredoxin Oxidoreductase Protein, subunit A, domain 3; 1.
DR Gene3D; 3.60.9.10; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
DR InterPro; IPR013984; Ald_Fedxn_OxRdtase_dom2.
DR InterPro; IPR013985; Ald_Fedxn_OxRdtase_dom3.
DR InterPro; IPR013983; Ald_Fedxn_OxRdtase_N.
DR InterPro; IPR036503; Ald_Fedxn_OxRdtase_N_sf.
DR InterPro; IPR001203; OxRdtase_Ald_Fedxn_C.
DR InterPro; IPR036021; Tungsten_al_ferr_oxy-like_C.
DR PANTHER; PTHR30038; ALDEHYDE FERREDOXIN OXIDOREDUCTASE; 1.
DR PANTHER; PTHR30038:SF7; TUNGSTEN-CONTAINING GLYCERALDEHYDE-3-PHOSPHATE:FERREDOXIN OXIDOREDUCTASE; 1.
DR Pfam; PF01314; AFOR_C; 1.
DR Pfam; PF02730; AFOR_N; 1.
DR SMART; SM00790; AFOR_N; 1.
DR SUPFAM; SSF48310; Aldehyde ferredoxin oxidoreductase, C-terminal domains; 1.
DR SUPFAM; SSF56228; Aldehyde ferredoxin oxidoreductase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABW02627.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001137}.
FT DOMAIN 13..215
FT /note="Aldehyde ferredoxin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00790"
SQ SEQUENCE 614 AA; 68092 MW; FFF518EAB8EE24EF CRC64;
MPTQHQMPRL FGWVGKVVEV DLSSGGIKTL TLDAEVYDKV LGGEGLAAYF IYKNFHEIRG
PLDPSNIIVF ASGPLTSEII PQSGRLSAAF ISPLTGIFGA THIGTRFAYE LKRAGYDAVI
VKGASEKPVY IYIEGDHVEI RGAEKYWGLD IMETVNSIKK DLGDPSIKAI AIGPAGEHLV
KFSTIANEEG IGGRTGGGAV MGSKKLKAIV VKGVEDISMA DPEGLRRYVR DLNVKLASST
RGASFRRYGS AGTVNLYHQI GNLPIKNFAW GRWNDDEVFK ISGEKLTETF LKRPFPCTTC
PVACKRYVEV KPGSKYFPGG FRGLGPEYET LALLGSNLLN SDLEAMIKIN ELCDKLGLDT
MSTGNVIGFI FEAAEKGLIN KEVDGLRLEW GNADTIIKLV QKIAYRDGIG DLLAEGVRRV
SERIGGREFA MHIKGLEVPA HDGRAFFAHA LSFMTMNRGA DHLGFTHIPW RGIPIPELGI
NARTDRYNES DEMVDIVINI QNLMVVYDSL TMCKYAHFAG LTITDIINLL KLTTGKDYTV
EKILEIGGRI WKIERWINNQ LGITRKDDVL PPRMLTPHEK RDDTKIPRIV EKWLPLYYRK
RGLTEDGIVK ELDI
//
